7ko3: Difference between revisions
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==Dihydrodipicolinate synthase (DHDPS) from C.jejuni, E88D mutant with pyruvate bound in the active site and L-lysine bound at the allosteric site== | |||
<StructureSection load='7ko3' size='340' side='right'caption='[[7ko3]], [[Resolution|resolution]] 2.22Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7ko3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni_subsp._jejuni_NCTC_11168_=_ATCC_700819 Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KO3 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.22Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7ko3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ko3 OCA], [https://pdbe.org/7ko3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ko3 RCSB], [https://www.ebi.ac.uk/pdbsum/7ko3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ko3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DAPA_CAMJE DAPA_CAMJE] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418] | |||
==See Also== | |||
*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]] | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Majdi Yazdi M]] | ||
[[Category: Sanders DAR]] | |||
[[Category: Saran S]] | |||
Latest revision as of 18:29, 18 October 2023
Dihydrodipicolinate synthase (DHDPS) from C.jejuni, E88D mutant with pyruvate bound in the active site and L-lysine bound at the allosteric siteDihydrodipicolinate synthase (DHDPS) from C.jejuni, E88D mutant with pyruvate bound in the active site and L-lysine bound at the allosteric site
Structural highlights
FunctionDAPA_CAMJE Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418] See Also |
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